Title : Solution structural analysis of the single-domain parvulin TbPin1.

Pub. Date : 2012

PMID : 22900083






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 TbPin1 was identified as a novel class of Pin1-type parvulins from Trypanosoma brucei, containing a unique PPIase domain, which can catalyze the isomerization of phosphorylated Ser/Thr-Pro peptide bond. Serine FKBP prolyl isomerase 1B Homo sapiens
2 TbPin1 was identified as a novel class of Pin1-type parvulins from Trypanosoma brucei, containing a unique PPIase domain, which can catalyze the isomerization of phosphorylated Ser/Thr-Pro peptide bond. Threonine FKBP prolyl isomerase 1B Homo sapiens
3 TbPin1 was identified as a novel class of Pin1-type parvulins from Trypanosoma brucei, containing a unique PPIase domain, which can catalyze the isomerization of phosphorylated Ser/Thr-Pro peptide bond. Proline FKBP prolyl isomerase 1B Homo sapiens